NSE5_YEAST
ID NSE5_YEAST Reviewed; 556 AA.
AC Q03718; D6VZF1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Non-structural maintenance of chromosome element 5;
DE Short=Non-SMC element 5;
GN Name=NSE5; OrderedLocusNames=YML023C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS], AND INTERACTION WITH KRE29.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP SUBUNIT.
RX PubMed=15738391; DOI=10.1073/pnas.0500537102;
RA Zhao X., Blobel G.;
RT "A SUMO ligase is part of a nuclear multiprotein complex that affects DNA
RT repair and chromosomal organization.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4777-4782(2005).
CC -!- FUNCTION: Acts in a DNA repair pathway for removal of UV-induced DNA
CC damage that is distinct from classical nucleotide excision repair and
CC in repair of ionizing radiation damage. Functions in homologous
CC recombination repair of DNA double strand breaks and in recovery of
CC stalled replication forks.
CC -!- SUBUNIT: Component of the Smc5-Smc6 complex which consists of KRE29,
CC MMS21, NSE1, NSE3, NSE4, NSE5, SMC5 and SMC6. Interacts with KRE29.
CC {ECO:0000269|PubMed:14690591, ECO:0000269|PubMed:15738391}.
CC -!- INTERACTION:
CC Q03718; P40026: KRE29; NbExp=3; IntAct=EBI-27756, EBI-22506;
CC Q03718; Q08204: SMC5; NbExp=3; IntAct=EBI-27756, EBI-34125;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14690591}. Chromosome
CC {ECO:0000250|UniProtKB:O94668}.
CC -!- MISCELLANEOUS: Present with 907 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z46659; CAA86632.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09875.1; -; Genomic_DNA.
DR PIR; S49754; S49754.
DR RefSeq; NP_013689.1; NM_001182381.1.
DR PDB; 7LTO; EM; 3.20 A; A=1-556.
DR PDB; 7OGG; X-ray; 3.29 A; R=1-556.
DR PDB; 7SDE; EM; 3.20 A; A=1-556.
DR PDBsum; 7LTO; -.
DR PDBsum; 7OGG; -.
DR PDBsum; 7SDE; -.
DR AlphaFoldDB; Q03718; -.
DR SMR; Q03718; -.
DR BioGRID; 35146; 456.
DR ComplexPortal; CPX-1364; SMC5-SMC6 SUMO ligase complex.
DR DIP; DIP-4547N; -.
DR IntAct; Q03718; 28.
DR STRING; 4932.YML023C; -.
DR iPTMnet; Q03718; -.
DR MaxQB; Q03718; -.
DR PaxDb; Q03718; -.
DR PRIDE; Q03718; -.
DR EnsemblFungi; YML023C_mRNA; YML023C; YML023C.
DR GeneID; 854985; -.
DR KEGG; sce:YML023C; -.
DR SGD; S000004485; NSE5.
DR VEuPathDB; FungiDB:YML023C; -.
DR eggNOG; ENOG502QU63; Eukaryota.
DR HOGENOM; CLU_035923_0_0_1; -.
DR InParanoid; Q03718; -.
DR OMA; LLRCQLF; -.
DR BioCyc; YEAST:G3O-32625-MON; -.
DR PRO; PR:Q03718; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03718; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:0016925; P:protein sumoylation; IC:ComplexPortal.
DR GO; GO:0032204; P:regulation of telomere maintenance; IC:ComplexPortal.
DR InterPro; IPR014803; DNA_repair_Nse5/Nse6.
DR Pfam; PF08691; Nse5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; DNA damage; DNA recombination; DNA repair;
KW Nucleus; Reference proteome.
FT CHAIN 1..556
FT /note="Non-structural maintenance of chromosome element 5"
FT /id="PRO_0000057963"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:7OGG"
FT HELIX 26..40
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:7LTO"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:7LTO"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:7LTO"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:7LTO"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:7OGG"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:7LTO"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:7OGG"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:7OGG"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:7OGG"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:7LTO"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:7LTO"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 240..254
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 269..275
FT /evidence="ECO:0007829|PDB:7SDE"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:7SDE"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:7LTO"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 294..301
FT /evidence="ECO:0007829|PDB:7LTO"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:7LTO"
FT TURN 323..326
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 340..362
FT /evidence="ECO:0007829|PDB:7LTO"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:7LTO"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 395..402
FT /evidence="ECO:0007829|PDB:7LTO"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:7LTO"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:7OGG"
FT HELIX 414..429
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:7SDE"
FT HELIX 445..449
FT /evidence="ECO:0007829|PDB:7SDE"
FT HELIX 452..456
FT /evidence="ECO:0007829|PDB:7SDE"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:7SDE"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:7SDE"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:7SDE"
FT HELIX 472..495
FT /evidence="ECO:0007829|PDB:7SDE"
FT HELIX 501..510
FT /evidence="ECO:0007829|PDB:7LTO"
FT HELIX 519..528
FT /evidence="ECO:0007829|PDB:7SDE"
FT HELIX 540..546
FT /evidence="ECO:0007829|PDB:7SDE"
SQ SEQUENCE 556 AA; 64013 MW; 6680A04D91E537DD CRC64;
MDGALINSVL YVSPRNGAHY FVELTEKHLL AFEMLNSMCL LENYDHVLLF LECQFGKSHN
LAVIPFDIIL VLFTLSTLSE YYKEPILRAN DPYNTSRETL SRRALKLLQK YLAILKEFDS
EQYNLYDLEL LRCQFFLAID TLTPKKQKWG FDRFRRTKSE SGVTYRQNAS VDPELDQAKT
FKNPYRSYIS CLEQRNTILG NRLLNLKLNE PGEFINMILW TLSNSLQEST PLFLSSHEIW
MPLLEILIDL FSCRQDYFIQ HEVAQNVSKS LFVQRLSESP LAVFFESLNT RNFANRFSEY
VFLNCDYKLP SDNYATPVHP VYNGENTIVD TYIPTIKCSP LYKSQKSLAL RRKLIGSCFK
LLLRVPDGHR LITPRIVADD VIQGISRTLA SFNDILQFKK FFMTENLSQE SYFIPLLAEG
TLSEILKDTQ ECVVILTLVE NLSDGVSFCN EVIGLVKSKC FAFTEQCSQA SYEEAVLNIE
KCDVCLLVLL RYLLHLIGTE AILDAKEQLE MLHAIEKNDS GRRQWAKALN LGNDPPLLYP
IVSQMFGVHD KSVIIE
